ArticleEBioMedicine2025
Mapping the antibody response to Lassa virus vaccination of non-human primates.
Article in EBioMedicine, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- Immunogenicity of recombinant vesicular stomatitis virus-vectored vaccines expressing the Machupo virus glycoprotein in different genome positions.Journal of virology · 2026Article
- B cell immunity to the Lassa virus glycoprotein is a correlate of vaccination-induced virus control in mice.Nature communications · 2026Article
- Comparison of Vaccine Platforms for Machupo Virus.Vaccines · 2026Article
- A multi-epitope vaccine targetingFrontiers in immunology · 2026Article
- Infusion of neutralization into Lassa vaccine design.Trends in immunology · 2025Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundLassa fever, caused by Lassa virus, is a severe disease, endemic in Western Africa, for which no vaccines or therapeutics are yet approved. Understanding the immune responses elicited by candidate vaccines is key for approval, including characterisation of antibody epitopes recognised and capacity for neutralisation.
methodsHere we used negative-stain electron microscopy polyclonal antibody epitope mapping (EMPEM), in-vitro pseudovirus neutralisation assays, and biophysical antibody competition assays to uncover components of polyclonal antibody responses elicited in nonhuman primates 26 days after receipt of a single immunisation with a fully protective, recombinant, replication-competent vesicular stomatitis virus-based vaccine bearing the Lassa virus glycoprotein GPC.
findingsAlthough the vaccinee sera are overall poorly-neutralising, we do directly visualise, within the polyclonal pool, antibodies targeting epitopes on GPC that are consistent with neutralisation, as well as competition with known neutralising mAbs. Nearly every animal, for example, produced antibodies that compete with mAbs against GP1-A and GPC-A neutralising epitopes. The most abundant classes of antibodies, however, are directed against interior interfaces of GPC, while other antibodies recognise post-fusion GPC epitopes not consistent with neutralisation.
interpretationIt may be that some individual antibodies in the pool are neutralising, but that the abundance of non-neutralising epitopes reduces potency as measured at the polyclonal level. The finding, however, neutralisation-consistent sites and competition with known neutralising antibodies are important steps in vaccine design toward eliciting more potent neutralisation.
fundingA complete list of funding bodies that supported this study is presented in the Funding section.
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